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Literature summary for 1.13.11.34 extracted from
- Identification of the substrate access portal of 5-lipoxygenase (2015), Biochemistry, 54, 6333-6342 .
Application
| Application | Comment | Organism |
|---|---|---|
| drug development | 5-lipoxygenase (5-LOX) is a target for drug design. Due to its role in the production of inflammatory lipid mediators, 5-LOX is a target for the development of therapeutics for conditions as diverse as asthma, cardiovascular disease, pancreatic cancer, and traumatic brain injury | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ALOX5, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Rosetta2 | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| A603L | site-directed mutagenesis, almost inactive mutant | Homo sapiens |
| A603L/Y181A | site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme | Homo sapiens |
| C240A | site-directed mutagenesis, the mutation renders the enzyme less susceptible to product inactivation | Homo sapiens |
| C561A | site-directed mutagenesis, the mutation renders the enzyme less susceptible to product inactivation | Homo sapiens |
| D170S/G174N | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Homo sapiens |
| F177A | site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme | Homo sapiens |
| F177A/Y181A | site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme | Homo sapiens |
| F177A/Y181A/H600V | site-directed mutagenesis, the mutant shows about 50% reduced activity compared to the wild-type enzyme | Homo sapiens |
| G174N | site-directed mutagenesis, inactive mutant | Homo sapiens |
| H600A | site-directed mutagenesis, inactive mutant | Homo sapiens |
| W147L | site-directed mutagenesis, inactive mutant | Homo sapiens |
| Y181A | site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate | product inhibition | Homo sapiens |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | a non-heme iron dioxygenase | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arachidonate + O2 | Homo sapiens | - |
(5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P09917 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Rosetta2 by cobalt affinity chromatography and ultrafiltration | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| arachidonate + O2 | - |
Homo sapiens | (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O | - |
? | |
| arachidonate + O2 | product generation is both regiospecific and stereospecific, the S-isomer is produced | Homo sapiens | (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 5-lipoxygenase | - |
Homo sapiens |
| 5-LOX | - |
Homo sapiens |
| ALOX5 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | structure-function analysis, overview. 5-LOX reveals a fully encapsulated active site, amino acid residue Phe177 plays a critical role in providing a fully functional active site, it shields the active site in the absence of substrate serving as the active site portal. Role for His600, deep in the elongated cavity, in positioning the substrate for catalysis | Homo sapiens |
| physiological function | the enzyme initiates the synthesis of pro-inflammatory leukotrienes and catalyze the peroxidation of polyunsaturated fatty acids | Homo sapiens |
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